During this grant period, we have continued our research in the area of the conformational analysis of biopolymer model systems. Specifically, we have carried out work using alanine polymers and oligomers to examine the helix-coil transition induced by trifluoroacetic acid. Our efforts included investigation of monodisperse oligopeptides and a nearly monodisperse icosimer (20-Mer). We have shown that the double peaks which are exhibited by these peptides in solution for the NH and alpha-CH protons can arise from folded forms which aggregate. In a related series of experiments, we have examined the spectral characteristics for poly((S)-beta-amino butyric acid), an optically active analog of poly beta-alanine. Circular dichroism and ultraviolet spectroscopy results indicate that the polymer prefers a beta-type structure in solution when the solvent is weakly interacting. Strong acids convert this polyamide into a random coil structure. In the solid state poly((S)-beta-amino butyric acid) exists primarily as an antiparallel beta-structure. These findings are supported by X-ray work in other laboratories.